title: The conformational changes analysis of maltodextrin binding protein based on elastic network model.
abstract: Maltodextrin Binding Protein (MBP) has provided a model system for investigating open-closed conformation transition based on two coarse-grained elastic network models. GNM results show that the open and closed forms have the same motion hinge axes and the open-closed conformational transition mainly exhibits as a large movement of the N-domain. ANM calculation shows a transition from open/closed to closed/open, which is helpful for ligand binding or release. During the open-closed transition, the residues within the domains move in a highly coupled way, and this indicates that the hinge connecting the domains is flexible, while the domains themselves are rigid.
authors.affiliation: Shandong Provincial Key Laboratory of Functional Macromolecular Biophysics, Dezhou University, Physics Department, Dezhou University, Dezhou, Shandong 253023, China. tianwaifeixian78@163.com
authors.forename: Haiyan
authors.initials: H
authors.lastname: Li
authors.forename: Jihua
authors.initials: J
authors.lastname: Wang
mesh_terms: D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D033902:Periplasmic Binding Proteins; D011487:Protein Conformation
chemical_list: D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008024:Ligands; C461619:MalE protein, E coli; D033902:Periplasmic Binding Proteins